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Tryptathionine bridges in peptide synthesis
Author(s) -
May Jonathan P.,
Perrin David M.
Publication year - 2007
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.20807
Subject(s) - chemistry , peptide , preprint , affinities , binding affinities , computational biology , cysteine , stereochemistry , combinatorial chemistry , biochemistry , biology , computer science , world wide web , receptor , enzyme
Abstract The tryptathionine linkage is a crosslink formed between tryptophan and cysteine. This feature is characteristic of the bicyclic peptides: the phallotoxins and the amatoxins. These peptides both bind to protein folds of their respective targets (F‐actin and RNA pol II, respectively) with extremely high affinities. Studies on these peptides have shown that the tryptathionine crosslink is essential for this binding affinity. Tryptathionines have been investigated for many years and several syntheses exist for their formation. In this review, we report on the various methodologies employed in tryptathionine synthesis, and discuss some of the advantages and disadvantages associated with each of them. © 2007 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 88: 714–724, 2007. This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com